Streptomyces lincolnensis M-20 균주로부터 분리, 정제된 L-Asparaginase의 열안정성과 단백 가수 분해 효소에 대한 저항성

• 영문명: Thermostability and Resistance to Proteolysis of L-Asparaginase Purified from Streptomyces lincolnensis M-20
• 발행기관: 대한약학회
• 저자명: 김경자(Kyoung Ja Kim)
• 간행물 정보: 『약학회지』제51권 제3호 (2007년), 199~205쪽, 전체 7쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2007.06.30

영문 초록

Thermostable asparaginase was purified to homogeneity from mesophilic Streptomyces lincolnensis M-20 by 30~70% ammonium sulfate precipitation and asparagine-Sepharose CL 6B affinity column chromatography. The apparent molecular mass of L-asparaginase by SDS-PAGE was found to be 47 kDa, whereas by its mobility on Sephacryl S-300 column was around 180 kDa, indicating that the enzyme at the native stage acts as tetramer. The purified enzyme showed a single band on acrylamide gel electrophoresis. The optimum pH and temperature were pH 9.5 and 55℃, respectively. Chemical modification experiments of purified asparagines implied the existence cystein residue located at or near active site. Purified asparaginase retained the 85% of the initial activity after incubation at 90℃ for 30 min. A correlation between thermostability and resistance to proteolysis of commercial asparaginase and purifed asparaginase from Streptomyces lincolnensis M-20 was investigated. Purified thermostable asparaginase was resistant to trypsin and chymotrypsin treatment, while the commercial asparaginase was not thermostable and was susceptible to proteolytic treatment with trypsin and chymotrypsin.

키워드

themostability resistance to proteolysis asparaginase Streptomyces lincolnensis M-20